Reviewed, UniProtKB/Swiss-Prot B7NPC5 (TDH_ECO7I)

Names and origin

Protein names

Recommended name:
    L-threonine 3-dehydrogenase
    EC=1.1.1.103

Gene names

Name:	tdh
Ordered Locus Names:	ECIAI39_4137

Organism

Escherichia coli O7:K1 (strain IAI39 / ExPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585057 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. HAMAP MF_00627
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. HAMAP MF_00627
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW threonine catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-threonine 3-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	L-threonine 3-dehydrogenase HAMAP MF_00627		PRO_1000130546
Sites
	Metal binding	38	1	Zinc 1; catalytic By similarity
	Metal binding	63	1	Zinc 1; catalytic By similarity
	Metal binding	93	1	Zinc 2 By similarity
	Metal binding	96	1	Zinc 2 By similarity
	Metal binding	99	1	Zinc 2 By similarity
	Metal binding	107	1	Zinc 2 By similarity
	Metal binding	148	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7NPC5-1 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: AAB2927DC7E01C1E	FASTA	341	37,285
	10 20 30 40 50 60 MKALSKLKAE EGIWMTDVPV PELGHNDLLI KIRKTAICGT DVHIYNWDEW SQKTIPVPMV 70 80 90 100 110 120 VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR GGRTHLCRNT IGVGVNRPGC 130 140 150 160 170 180 FAEYLVIPAF NAFKIPDNIS DDLASIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA 190 200 210 220 230 240 AVAKHVGARN VVITDVNEYR LELARKMGIT RAVNVAKENL NDVMTELGMT EGFDVGLEMS 250 260 270 280 290 300 GAPPAFRTML DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA 310 320 330 340 LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU928164 Genomic DNA. Translation: CAR20245.1.
RefSeq	YP_002410014.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7154157.
GenomeReviews	Gene locus ECIAI39_4137 in contig CU928164_GR.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00627. [Tree]
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. IPR004627. L-Threonine_3-DHase. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00692. tdh. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TDH_ECO7I

Accession

Primary (citable) accession number: B7NPC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	March 24, 2009
Last modified:	September 22, 2009
This is version 6 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)